NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1159/000079829; PubMed=15383718 [NCBI, ExPASy, EBI, Israel, Japan]
Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P., Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.;
"The complete genome sequence of Bacillus licheniformis DSM13, an organism with great industrial potential.";
J. Mol. Microbiol. Biotechnol. 7:204-211(2004).

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1186/gb-2004-5-10-r77; PubMed=15461803 [NCBI, ExPASy, EBI, Israel, Japan]
Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J., Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B., Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A., Bolotin A., Lapidus A., Galleron N., Ehrlich S.D., Berka R.M.;
"Complete genome sequence of the industrial bacterium Bacillus licheniformis and comparisons with closely related Bacillus species.";
Genome Biol. 5:RESEARCH077.1-RESEARCH077.12(2004).

Comments

FUNCTION: Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine (By similarity).
CATALYTIC ACTIVITY: L-histidinol + 2 NAD⁺ = L-histidine + 2 NADH.
COFACTOR: Binds 1 zinc ion per subunit (By similarity).
PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9 .
SIMILARITY: Belongs to the histidinol dehydrogenase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AE017333; AAU42555.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
CP000002; AAU25184.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_080822.1; -.
YP_093248.1; -.

3D structure databases

ModBase

Q65EF9.

Enzyme and pathway databases

BioCyc

BLIC279010:BL03408-MON; -.

Ontologies

GO:0004399;	Molecular function: histidinol dehydrogenase activity (inferred from electronic annotation from HAMAP).
GO:0000105;	Biological process: histidine biosynthetic process (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_01024; -; 1.
PBIL [Tree]

InterPro

IPR001692; Histidinol_DHase.
IPR012131; Hstdl_DHase_prok.
Graphical view of domain structure.

PANTHER

PTHR21256:SF2; Hstdl_DH_prok; 1.

Pfam

PF00815; Histidinol_dh; 1.
Pfam graphical view of domain structure.

PRINTS

PR00083; HOLDHDRGNASE.

ProDom

PD002680; Histidinol_dh; 1.
[Domain structure / List of seq. sharing at least 1 domain]

TIGRFAMs

TIGR00069; hisD; 1.

PROSITE

PS00611; HISOL_DEHYDROGENASE; 1.

BLOCKS

Q65EF9.

Genome annotation databases

GeneID

3027872; -.
3100933; -.

GenomeReviews

CP000002_GR; BL03408.
AE017333_GR; BLi03736.

KEGG

bld:BLi03736; -.
bli:BL03408; -.

NMPDR

fig|279010.5.peg.3801; -.

Phylogenomic databases

HOGENOM

Q65EF9; -.

Genome annotation databases

CMR

Q65EF9; BLi03736.

Other

ProtoNet

Q65EF9.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Amino-acid biosynthesis; Complete proteome; Histidine biosynthesis; Metal-binding; NAD; Oxidoreductase; Zinc.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 426`	`426`	`Histidinol dehydrogenase.`	`PRO_0000135727`
`ACT_SITE`	`321 321`		`Proton acceptor (By similarity).`
`ACT_SITE`	`322 322`		`Proton acceptor (By similarity).`
`METAL`	`253 253`		`Zinc (By similarity).`
`METAL`	`256 256`		`Zinc (By similarity).`
`METAL`	`355 355`		`Zinc (By similarity).`
`METAL`	`414 414`		`Zinc (By similarity).`
`BINDING`	`123 123`		`NAD (By similarity).`
`BINDING`	`185 185`		`NAD (By similarity).`
`BINDING`	`208 208`		`NAD (By similarity).`
`BINDING`	`231 231`		`Substrate (By similarity).`
`BINDING`	`253 253`		`Substrate (By similarity).`
`BINDING`	`256 256`		`Substrate (By similarity).`
`BINDING`	`322 322`		`Substrate (By similarity).`
`BINDING`	`355 355`		`Substrate (By similarity).`
`BINDING`	`409 409`		`Substrate (By similarity).`
`BINDING`	`414 414`		`Substrate (By similarity).`

Sequence information

Length: 426 AA [This is the length of the unprocessed precursor]

Molecular weight: 46028 Da [This is the MW of the unprocessed precursor]

CRC64: 76A087539E215CA8 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKIKSISGNT SVSLKRSIDA GTEEQRKAVR GIIEEVKKNG NAAVSAFTRQ FDGADVAGFR 

        70         80         90        100        110        120 
VSEEEIKEAY SALEERDLEI IQAAIFNIKE YHERQLATSW FYHRKDGTML GQKITPLDSA 

       130        140        150        160        170        180 
GVYVPGGTAA YPSSVLMNVI PALVAGVDRI VLASPPGKDG KLSAGVLAAA AELGVTEIYK 

       190        200        210        220        230        240 
MGGAQAIAAL AYGTETITPV DKITGPGNIY VALAKREVFG QVDIDMIAGP SEIAILADST 

       250        260        270        280        290        300 
ANYREIAADL LSQAEHDAMA SSILVTDSET LAESVLKEVY RQLEHLPRKE IARQSIDNYG 

       310        320        330        340        350        360 
LIYVTETMNE AVSVINELAP EHLEILTVQP DALLGQIKHA GAIFLGRYSS EPVGDYFAGP 

       370        380        390        400        410        420 
NHVLPTNGTA RFSSPLNVTD FQKRSSIISY SREAFRANAE KIAAFARLEG LEAHARAIES 


RNREED

Q65EF9 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools